文摘
The endo-inulinase gene (EnIA) from Arthrobacter sp. S37 was ligated into the expression vector pINA1317 and over-expressed in Yarrowia lipolytica Po1h. It was found that the endo-inulinase activity and specific endo-inulinase activity produced by the transformant 1317-EnIA were 16.7 U/mL and 93.4 U/mg, respectively. The recombinant EnIA was purified and characterized. The molecular weight of the purified rEnIA was 78.9 kDa. The optimal pH and temperature of the purified rEnIA were 4 and 50 ¡ãC, respectively. The purified rEnIA was stable in the temperature range of 4?0 ¡ãC and in the pH range of 2?. The activity of rEnIA was greatly stimulated in the presence of Li+. The purified rEnIA could actively convert inulin into disaccharides.